Specific Interactions of the Autoantigen L7 with Multi-zinc Finger Protein ZNF7 and Ribosomal Protein S7
| Autor: | Ulrich Krawinkel, Stephan Witte |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
Ribosomal Proteins
Zinc finger Leucine Zippers Leucine zipper RNF4 Kruppel-Like Transcription Factors Zinc Fingers Cell Biology Biology Biochemistry Molecular biology Cell biology DNA-Binding Proteins RING finger domain Jurkat Cells Ribosomal protein GATAD2B biology.protein Humans Protein G Dimerization Ribosomes Molecular Biology LIM domain |
| Zdroj: | Journal of Biological Chemistry. 272:22243-22247 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.272.35.22243 |
| Popis: | The eucaryotic protein L7, which associates with the large subunit of ribosomes, has been shown to be a major autoantigen in systemic autoimmune arthritis. The N terminus carries a sequence motif that is similar to the leucine zipper domain of eucaryotic transcription factors. This domain promotes the homodimerization of protein L7 through α-helical coiled-coil formation and binds to distinct mRNAs, thereby inhibiting their cell-free translation. Using a yeast two-hybrid selection, we have identified from a Jurkat T lymphoma cDNA library ribosomal protein S7 and the multi-zinc finger protein ZNF7 as proteins that interact with protein L7. A fragment of L7 carrying the leucine zipper-like domain is fully sufficient to mediate these interactions. Their potential biological significance is indicated by low apparent dissociation constants of S7-L7 (15 × 10−9 m) and, respectively, ZNF7-L7 (2 × 10−9 m) complexes and co-immunoprecipitation of proteins S7, ZNF7, and L7 from a cell lysate with an anti-L7 antibody. We also show that ZNF7-like L7 and S7 can exist in a ribosome-bound form. This study provides further evidence suggesting that L7 is involved in translational regulation through interactions with components of the translational apparatus. |
| Databáze: | OpenAIRE |
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